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PubMed · 7151171

The nuclear matrix: three-dimensional architecture and protein composition.

D G Capco·K M Wan·S Penman
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Abstract

The structural filament network of the nucleus is prepared while still connected to the cytoskeleton. The relatively gentle procedure removes about 98% of the DNA and at least 86% of the histones. The matrix is bounded by an outer nuclear lamina connected to the cytoskeletal framework, as well as the inner filaments. The filaments range in diameter from 3 to 22 nm, and are organized in a three-dimensional anastomosing network in which nucleoli are enmeshed. The nuclear matrix is separated from the cytoskeletal framework by a double detergent and then partitioned into a chromatin fraction and a matrix fraction by nuclease and high salt. Two-dimensional gel electrophoresis shows that the proteins of the cytoskeleton, chromatin and nuclear matrix are very different. A major protein found in all fractions cofocuses with actin. Vimentin is largely associated with the nuclear matrix, probably as a corona external of filaments.

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AnimalsCell NucleusChromatinCytoplasmDNAHistonesHumansIsoelectric PointMiceMicroscopy, ElectronMolecular WeightProteinsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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D G Capco, K M Wan, S Penman. 1982. The nuclear matrix: three-dimensional architecture and protein composition.. https://doi.org/10.1016/0092-8674(82)90446-9

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